Hsp20 is a mammalian small heat-shock protein family that is found most copiously in skeletal muscle and heart. The heat-shock proteins seem to act as chaperones that can protect other proteins against heat-induced denaturation and aggregation. The Hsp20 family is characterized structurally by the presence of a conserved C-terminal domain of about 100 residues and contains a beta-sandwich fold consisting of 8 strands in 2 beta-sheets in a "Greek-key" topology. Hsp20 proteins have a tendency to form dimers, through a disulphide linkage formed by an N-terminal cysteine, low heat stability and a poor chaperoning ability in comparison with other family members.

HSP20 although stable at 10°C for 2 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

Immunological Activity:

Immunoreactivity is confirmed by reaction with monoclonal mouse antibodies against HSP20.